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Limenin, a defensin‐like peptide with multiple exploitable activities from shelf beans
Author(s) -
Wong Jack H.,
Ng T. B.
Publication year - 2006
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.732
Subject(s) - fusarium oxysporum , peptide , botrytis cinerea , reticulocyte , biochemistry , thymidine , affinity chromatography , size exclusion chromatography , chemistry , lysis , microbiology and biotechnology , molecular mass , biology , in vitro , botany , enzyme , messenger rna , gene
Abstract From the seeds of the shelf bean, an antifungal peptide with a molecular mass of 6.5 kDa was isolated. The isolation procedure comprised affinity chromatography on Affi‐gel blue gel, ion exchange chromatography on Mono S, and gel filtration on Superdex 75. The peptide was adsorbed on Affi‐gel blue gel and Mono S. It potently suppressed mycelial growth in Botrytis cinerea, Fusarium oxysporum , and Mycosphaerella arachidicola with an IC 50 of 2.9, 2.1, and 0.34 µ M , respectively. It exerted antibacterial activity toward several bacterial species with an IC 50 approximating 100 µ M . [Methyl‐ 3 H]‐thymidine incorporation into isolated mouse splenocytes was stimulated. [Methyl‐ 3 H]‐thymidine incorporation into M1 (myeloma) and L1210 (leukemia) cells was inhibited. The peptide reduced the activity of HIV‐1 reverse transcriptase and also inhibited translation in a cell‐free rabbit reticulocyte lysate system. Copyright © 2005 European Peptide Society and John Wiley & Sons, Ltd.